5eob

Crystal structure of CMET in complex with novel inhibitor

Method: X-RAY DIFFRACTION Dmax: 74.9 Å Quality: REASONABLE

1. Protein Identity and Related Structures Protein Identity & Related Structures

Hepatocyte growth factor receptor

Homo sapiens

UniProt P08581

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1038–1346 Fragment:UNP residues 1038-1346 5QQ 6-[bis(fluoranyl)-[6-(4-fluorophenyl)-[1,2,4]triazolo[4,3-b][1,2,4]triazin-3-yl]methyl]quinoline × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;19-20%(w/v)PEG 3350, 200mM MgSO4, 100mM Tris-HCl Resolution 1.75 Å R-free 0.197

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

128 other PDB entries and 166 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MET_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 11–319; UniProt 1038–1346

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 5eob

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5eob
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5eob
Deposition date deposition_date2015-11-10
Structure title titleCrystal structure of CMET in complex with novel inhibitor
Keywords keywordsCMET inhibitor, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier20.59
Radius of gyration Rg (electron density) rg_electron19.64
Forward intensity I(0) i017305100.00
Molecular weight molecular_weight32460.0 kDa
Excluded volume excluded_volume41074 ų
Envelope volume envelope_volume47836 ų
Hydration-shell volume shell_volume20394 ų
Envelope diameter envelope_diameter66.8
Shell Rg shell_rg26.04
Envelope Rg envelope_rg20.05
Shape Rg shape_rg19.62
Total Rg total_rg20.62
Total atoms total_atoms2286
Residues n_residues288
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax74.9
Rg (real space) rg_real20.55
Rg uncertainty (real space) rg_real_error0.60
I(0) (real space) i0_real1.7310e+07
I(0) uncertainty (real space) i0_real_error2.5420e+05
Rg (reciprocal space) rg_reciprocal20.56
I(0) (reciprocal space) i0_reciprocal17310000.0000
Solution quality estimate total_estimate0.5817
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary23.9
Skewness Skewness skewness0.338
Kurtosis Kurtosis kurtosis-0.285
Angular range angular_range— – 0.3850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7443000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.626; Stabil: 1.000; Sysdev: 0.242; Positv: 1.000; Valcen: 0.951; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd5eoba_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.144 — Protein kinase-like (PK-like)
Superfamily Superfamily superfamilyd.144.1 — Protein kinase-like (PK-like)
Family Family familyd.144.1.7 — Protein kinases, catalytic subunit

CATH v4.4 (2 domains)

Domain ID domain_id5eobA01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology200 — Phosphorylase Kinase; domain 1
Homologous superfamily homologous superfamily20 — Phosphorylase Kinase; domain 1
Domain ID domain_id5eobA02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology510 — Transferase(Phosphotransferase); domain 1
Homologous superfamily homologous superfamily10 — Transferase(Phosphotransferase) domain 1

8. Citations (2)

9. Files and Curves (10)